PARP1 ART in complex with HPF1 and EB47. Determined by electron microscopy at 4.3 Å resolution. Released 21 Jan 2026.
Explore 9MJA in 3D Show helices and sheets RCSB PDB PDBe
9MJA contains 26 α-helices and 23 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 667-676 | 10 | |
| α-helix | 789-796 | 8 | |
| β-strand | 799-803 | 5 | 1 |
| α-helix | 804-805 | 2 | |
| α-helix | 809-820 | 12 | |
| β-strand | 829-841 | 13 | 1 |
| α-helix | 844-848 | 5 | |
| α-helix | 849-851 | 3 | |
| β-strand | 857-860 | 4 | 1 |
| β-strand | 861 | 1 | 2 |
| α-helix | 866-868 | 3 | |
| α-helix | 869-875 | 7 | |
| α-helix | 879-881 | 3 | |
| α-helix | 886-888 | 3 | |
| β-strand | 895-897 | 3 | 3 |
| β-strand | 898 | 1 | 2 |
| α-helix | 901-905 | 5 | |
| α-helix | 906-908 | 3 | |
| β-strand | 911 | 1 | 4 |
| β-strand | 914 | 1 | 4 |
| β-strand | 916-925 | 10 | 1 |
| β-strand | 929-932 | 4 | 3 |
| β-strand | 947-950 | 4 | 3 |
| β-strand | 954-955 | 2 | 5 |
| β-strand | 962-964 | 3 | 1 |
| β-strand | 967-969 | 3 | 1 |
| β-strand | 975-976 | 2 | 5 |
| β-strand | 986 | 1 | 5 |
| β-strand | 988-991 | 4 | 3 |
| β-strand | 998-1009 | 12 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 35-44 | 10 | |
| α-helix | 51-63 | 13 | |
| α-helix | 73-76 | 4 | |
| β-strand | 79-80 | 2 | 6 |
| α-helix | 83-87 | 5 | |
| β-strand | 115-120 | 6 | 6 |
| β-strand | 127-132 | 6 | 6 |
| β-strand | 142-147 | 6 | 6 |
| β-strand | 155-156 | 2 | 6 |
| α-helix | 161-175 | 15 | |
| α-helix | 179-199 | 21 | |
| α-helix | 208-215 | 8 | |
| α-helix | 245-257 | 13 | |
| α-helix | 261-267 | 7 | |
| α-helix | 269-283 | 15 | |
| α-helix | 287-300 | 14 | |
| α-helix | 303-305 | 3 | |
| α-helix | 306-319 | 14 | |
| α-helix | 323-334 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Poly [ADP-ribose] polymerase 1 | A | protein | 1034 | Homo sapiens | P09874 (AlphaFold model) |
| Histone PARylation factor 1 | B | protein | 347 | Homo sapiens | Q9NWY4 (AlphaFold model) |
>9MJA_1 Poly [ADP-ribose] polymerase 1 (chains A) MGSSHHHHHHSSGLVPRGSHMAESSDKLYRVEYAKSGRASCKKCSESIPKDSLRMAIMVQ SPMFDGKVPHWYHFSCFWKVGHSIRHPDVEVDGFSELRWDDQQKVKKTAEAGGVTGKGQD GIGSKAEKTLGDFAAEYAKSNRSTCKGCMEKIEKGQVRLSKKMVDPEKPQLGMIDRWYHP GCFVKNREELGFRPEYSASQLKGFSLLATEDKEALKKQLPGVKSEGKRKGDEVDGVDEVA KKKSKKEKDKDSKLEKALKAQNDLIWNIKDELKKVCSTNDLKELLIFNKQQVPSGESAIL DRVADGMVFGALLPCEECSGQLVFKSDAYYCTGDVTAWTKCMVKTQTPNRKEWVTPKEFR EISYLKKLKVKKQDRIFPPETSASVAATPPPSTASAPAAVNSSASADKPLSNMKILTLGK LSRNKDEVKAMIEKLGGKLTGTANKASLCISTKKEVEKMNKKMEEVKEANIRVVSEDFLQ DVSASTKSLQELFLAHILSPWGAEVKAEPVEVVAPRGKSGAALSKKSKGQVKEEGINKSE KRMKLTLKGGAAVDPDSGLEHSAHVLEKGGKVFSATLGLVDIVKGTNSYYKLQLLEDDKE NRYWIFRSWGRVGTVIGSNKLEQMPSKEDAIEHFMKLYEEKTGNAWHSKNFTKYPKKFYP LEIDYGQDEEAVKKLTVNPGTKSKLPKPVQDLIKMIFDVESMKKAMVEYEIDLQKMPLGK LSKRQIQAAYSILSEVQQAVSQGSSDSQILDLSNRFYTLIPHDFGMKKPPLLNNADSVQA KVEMLDNLLDIEVAYSLLRGGSDDSSKDPIDVNYEKLKTDIKVVDRDSEEAEIIRKYVKN THATTHNAYDLEVIDIFKIEREGECQRYKPFKQLHNRRLLWHGSRTTNFAGILSQGLRIA PPEAPVTGYMFGKGIYFADMVSKSANYCHTSQGDPIGLILLGEVALGNMYELKHASHISK LPKGKHSVKGLGKTTPDPSANISLDGVDVPLGTGISSGVNDTSLLYNEYIVYDIAQVNLK YLLKLKFNFKTSLW
>9MJA_2 Histone PARylation factor 1 (chains B) SMVGGGGKRRPGGEGPQCEKTTDVKKSKFCEADVSSDLRKEVENHYKLSLPEDFYHFWKF CEELDPEKPSDSLSASLGLQLVGPYDILAGKHKTKKKSTGLNFNLHWRFYYDPPEFQTII IGDNKTQYHMGYFRDSPDEFPVYVGINEAKKNCIIVPNGDNVFAAVKLFLTKKLREITDK KKINLLKNIDEKLTEAARELGYSLEQRTVKMKQRDKKVVTKTFHGAGLVVPVDKNDVGYR ELPETDADLKRICKTIVEAASDEERLKAFAPIQEMMTFVQFANDECDYGMGLELGMDLFC YGSHYFHKVAGQLLPLAYNLLKRNLFAEIIEEHLANRSQENIDQLAA
| ID | Name | Formula | Copies |
|---|---|---|---|
| UHB | 2-[4-[(2S,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]carbonyl… | C24 H27 N9 O6 | 1 |
PARP1-HPF1 structure and dynamics on nicked DNA suggest a mechanism for acute and localized ADP-ribosylation. Sverzhinsky, A., Xue, H., Langelier, M.F. et al. Nat Commun (2026) 17. DOI 10.1038/s41467-026-69375-3 · PubMed
Other PDB entries of the same protein (UniProt P09874 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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